ViMRT
}  
 
Home   
< Docs   

 HIV mutation literature information.


  Antiretroviral genotypic resistance mutations in HIV-1 infected Korean patients with virologic failure.
 PMID: 19949656       2009       Journal of Korean medical science
Result: M41L, I54V, D30N, and V82A/T/S were observed in more than 10 patients and K103N (10/41, 24.4%) was the most frequently observed NNRTI associated mutation.


  Genotypic resistance profiles in antiretroviral-naive HIV-1 infections before and after initiation of first-line HAART: impact of polymorphism on resistance to therapy.
 PMID: 18182278       2008       International journal of antimicrobial agents
Abstract: Moreover, major mutations (D30N and N88D) conferring resistance to PIs were found in patients infected with subtype B strain.


  Combination of non-natural D-amino acid derivatives and allophenylnorstatine-dimethylthioproline scaffold in HIV protease inhibitors have high efficacy in mutant HIV.
 PMID: 18426195       2008       Journal of medicinal chemistry
Abstract: Interestingly, anti-HIV activity of all the D-amino acid-introduced inhibitors was remarkably enhanced in their anti-HIV activities against a Nelfinavir-resistant clone, which has a D30N mutation in the protease, over that of the wild-type strain.


  Prevalence of resistance-associated mutations in human immunodeficiency virus type 1-positive individuals failing HAART in Rio de Janeiro, Brazil.
 PMID: 19219276       2008       The Brazilian journal of infectious diseases
Abstract: The most prevalent resistance mutations were: M184V (60.7%), T215Y (49.6%) and M41L (46.7%) in the RT gene and L90M (19.6%), M46I (16.2%) and D30N (12.8%) in the PR gene.


  HIV-1 protease catalytic efficiency effects caused by random single amino acid substitutions.
 PMID: 17090696       2007       Molecular biology and evolution
Abstract: In particular, the mutation N88D, lethal for the wild-type protease, restored the wild-type catalytic efficiency when combined with the highly deleterious mutation D30N.
Abstract: When a second random mutagenesis library was constructed from an HIV-1 protease carrying a highly deleterious single mutation (D30N), a higher proportion of mutations with neutral or beneficial effect were found, 26% and 9%, respectively.


  Natural polymorphisms in the human immunodeficiency virus type 2 protease can accelerate time to development of resistance to protease inhibitors.
 PMID: 17116674       2007       Antimicrobial agents and chemotherapy
Abstract: In contrast, no major PI mutations were selected in HIV-1 over this period except for D30N in the context of NFV selective pressure.


  Genotypic resistance in plasma and peripheral blood lymphocytes in a group of naive HIV-1 patients.
 PMID: 17306618       2007       Journal of clinical virology
Abstract: In addition, major mutations (D30N, M46I, I50V, I84V) associated with drug resistance in the PR region were only found in PBMCs.


  Mechanism of drug resistance due to N88S in CRF01_AE HIV-1 protease, analyzed by molecular dynamics simulations.
 PMID: 17367119       2007       Journal of medicinal chemistry
Abstract: Both D30N and N88S confer resistance against NFV.
Abstract: Patients in whom NFV treatment has failed predominantly carry D30N mutants of HIV-1 PRs if they have been infected with the subtype B virus.
Abstract: We also investigated why the emergence rates of D30N and N88S differ between subtype B and CRF01_AE HIV-1.


  HIV-1 subtype B protease and reverse transcriptase amino acid covariation.
 PMID: 17500586       2007       PLoS computational biology
Abstract: Patterns of protease covariation were dominated by the clustering of nelfinavir-associated mutations (D30N and N88D), two main groups of protease inhibitor (PI)-resistance mutations associated either with V82A or L90M, and a tight cluster of mutations associated with decreased susceptibility to amprenavir and the most recently approved PI darunavir.
Discussion: Protease covariation was dominated by the clustering of nelfinavir-associated mutations (D30N and N88D), two main groups of PI-resistance mutations associated either with V82A


  Computational characterization of structural role of the non-active site mutation M36I of human immunodeficiency virus type 1 protease.
 PMID: 17524421       2007       Journal of molecular biology
Abstract: The reason for the rare emergence of D30N variants in non-subtype B HIV-1 proteases was also clarified from our computational analysis.



Browser Board

 Co-occurred Entities




   Filtrator